ID Q2H8U5_CHAGB Unreviewed; 1016 AA.
AC Q2H8U5;
DT 21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 105.
DE RecName: Full=1-phosphatidylinositol 4-kinase {ECO:0000256|ARBA:ARBA00012169};
DE EC=2.7.1.67 {ECO:0000256|ARBA:ARBA00012169};
GN ORFNames=CHGG_03359 {ECO:0000313|EMBL:EAQ91424.1};
OS Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS NRRL 1970) (Soil fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX NCBI_TaxID=306901 {ECO:0000313|EMBL:EAQ91424.1, ECO:0000313|Proteomes:UP000001056};
RN [1] {ECO:0000313|Proteomes:UP000001056}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970
RC {ECO:0000313|Proteomes:UP000001056};
RX PubMed=25720678; DOI=10.1128/genomeA.00021-15;
RA Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL Genome Announc. 3:E0002115-E0002115(2015).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = a
CC 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) + ADP +
CC H(+); Xref=Rhea:RHEA:19877, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57880, ChEBI:CHEBI:58178, ChEBI:CHEBI:456216;
CC EC=2.7.1.67; Evidence={ECO:0000256|ARBA:ARBA00001686};
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DR EMBL; CH408030; EAQ91424.1; -; Genomic_DNA.
DR RefSeq; XP_001229875.1; XM_001229874.1.
DR AlphaFoldDB; Q2H8U5; -.
DR STRING; 306901.Q2H8U5; -.
DR GeneID; 4388639; -.
DR VEuPathDB; FungiDB:CHGG_03359; -.
DR eggNOG; KOG0903; Eukaryota.
DR HOGENOM; CLU_002446_2_0_1; -.
DR InParanoid; Q2H8U5; -.
DR OMA; TQDYVDV; -.
DR OrthoDB; 147843at2759; -.
DR Proteomes; UP000001056; Unassembled WGS sequence.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IEA:InterPro.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd05168; PI4Kc_III_beta; 1.
DR Gene3D; 6.10.140.1260; -; 1.
DR Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR021601; Phosphatidylino_kinase_fungi.
DR InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR InterPro; IPR036940; PI3/4_kinase_cat_sf.
DR InterPro; IPR018936; PI3/4_kinase_CS.
DR InterPro; IPR001263; PI3K_accessory_dom.
DR InterPro; IPR049160; PI4KB-PIK1_PIK.
DR InterPro; IPR015433; PI_Kinase.
DR PANTHER; PTHR10048:SF22; PHOSPHATIDYLINOSITOL 4-KINASE BETA; 1.
DR PANTHER; PTHR10048; PHOSPHATIDYLINOSITOL KINASE; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR Pfam; PF21245; PI4KB-PIK1_PIK; 1.
DR Pfam; PF11522; Pik1; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00916; PI3_4_KINASE_2; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
DR PROSITE; PS51545; PIK_HELICAL; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Reference proteome {ECO:0000313|Proteomes:UP000001056};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..120
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 698..1000
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT REGION 189..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 278..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 461..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..204
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 505..565
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1016 AA; 112694 MW; 04562B0F13B5B2D6 CRC64;
MSWDLLKRFL ESDVFNQNPF LSVSYLSRYA DHIGIHYVLC SKLRQFPYED IEFFLPQLCH
LIISVDNESM ALEEFLLDLC EESVTAALLT FWLFQTYLHD LAPNPQTEAF KTCRRVYNKV
QHVVFGISET VRQERITENV LPVTVLGSFV LASIACPLLP QWAGPLAIAQ ARKPRPVVEI
ISEPTAVTAK NNVPTRAHTI SASSTRSRRA KEGRSTSGQE GKTHASPRKS PGKLKLKTPR
PPSRSKTNES TPAPREQAEE ELPSHLENLA LEARISSASL PLPEHRPRLV TRPTTPVSAG
LRPSEAPRRH SHHVKTLLSQ GEMTQLQKTR LLRQNYFRCQ TAFLTALEDI SNRLVVVPKP
ARLSALRAEL ALIARDLPAE VDIPVLCPPN LVDGSPSRSR HHRIVRLNPA EATVLNSAEK
VPYLLMVEIL RDDFTFDPDT PDNQRLLTTL LDEQGTRKRI FDLSDSPSMP PASRAPEPVV
DSVFEPSSGD LGSSPMLRPE DDELFGTTPT QSHFSLRLSN NSTPAPASWD KTTTSRSSGG
SSESLSPPLN RRRLTLTNPR HNSVDQPDFS ALAVHMRTAS QMLAQLDATS GKRPRQEVAA
IRARIIASMQ SLEEQSFDLD DGQGPTFDTI MAKAQAAAVT AAATDAGGAE VAEDATVEPN
LNANAGIDRM ENDIKTGGLQ RKGDRDDPSA AVFGEAWETK KERIRKSSPY GWMKNWDLVS
VIIKTGSDLR QEAFACQLIR VCHKIWVDAG VPVWVKLMRI LVTGESSGLI ETIANGVSLH
SIKRSLTLAS IESGQNPRRR IATLKDHFVK AFGIPEGESF RAGVDAFKRS LAAYSVISYV
LQLKDRHNGN VLIDNEGHII HIDFGFMLSN SPGSVGFEAA PFKLTYEYVD VLGGVGSPDF
EDYKSLCKQA FQGMFVLPWW GTNECMLMWL VVCATALRRS ADNIIDLVSM MGRESKMPCF
GAGVTQVTTA LRQRFQLQLS ADEAEQFVET DLIAKALGSY YTRLYDTFQY RTQGIY
//
